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Protein Engineering vol. 4 no. 8 pp. 941-945, 1991
© 1991 Oxford University Press

RESEARCH-ARTICLE

Stabilization of the neutral protease of Bacillus stearothermophilus by removal of a buried water molecule

Gerrit Vriend, Herman J.C. Berendsen1, J. Rob van der Zee2, Bertus van der Burg2, Gerard Venema2 and Vincent G.H. Eijsink2,3

EMBL, BIOcomputing Program, Meyerhofstrasse 1, 6900 Heidelberg, Germany 1Department of Physical Chemistry, University of Groningen Nijenborgh 16, 9747 AG Groningen, The Netherlands 2Department of Genetics, Centre of Biological Sciences Kerklaan 30, 9751 NN Haren, The Netherlands

3To whom correspondence should be addressed

Using site-directed mutagenesis, Ala166 in the neutral protease of Bacillus stearothermophilus was changed into Ser. Model building and molecular dynamics simulations of the mutant enzyme indicated that the Ser hydroxyl group fits well in a cavity which contains a water molecule in the wild-type enzyme. The Alal66 - Ser mutation was expected to exert a stabilizing effect because of the gain in entropy resulting from the release of a water molecule from the folded protein to the solvent. In addition, the hydrogen-bonding network around residue 166 was improved upon the mutation. As a result of this mutation the thermostability of the neutral protease was increased by 1.2 ± 0.1°C.

Keywords: Bacillus/mutagenesis/neutral protease/thermostability/water

Received June 21, 1991; revised September 12, 1991;
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